ID A0A1J7GS65_LUPAN Unreviewed; 418 AA.
AC A0A1J7GS65;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN ORFNames=TanjilG_00166 {ECO:0000313|EMBL:OIV97137.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV97137.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV97137.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV97137.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
CC -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC {ECO:0000256|RuleBase:RU362087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-
CC protoporphyrin IX + phosphate; Xref=Rhea:RHEA:13961,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306,
CC ChEBI:CHEBI:60492, ChEBI:CHEBI:456216; EC=6.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001499,
CC ECO:0000256|RuleBase:RU362087};
CC -!- ACTIVITY REGULATION: Redox regulation; active in reducing conditions,
CC inactive in oxidizing conditions. {ECO:0000256|RuleBase:RU362087}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005173,
CC ECO:0000256|RuleBase:RU362087}.
CC -!- SUBUNIT: The magnesium chelatase complex is a heterotrimer consisting
CC of subunits CHLI, CHLD, AND CHLH. {ECO:0000256|RuleBase:RU362087}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU362087}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799, ECO:0000256|RuleBase:RU362087}.
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DR EMBL; CM007375; OIV97137.1; -; Genomic_DNA.
DR RefSeq; XP_019417706.1; XM_019562161.1.
DR AlphaFoldDB; A0A1J7GS65; -.
DR STRING; 3871.A0A1J7GS65; -.
DR EnsemblPlants; OIV97137; OIV97137; TanjilG_00166.
DR GeneID; 109328610; -.
DR Gramene; OIV97137; OIV97137; TanjilG_00166.
DR KEGG; lang:109328610; -.
DR OMA; QDEMKLA; -.
DR OrthoDB; 275672at2759; -.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000188354; Chromosome LG15.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.80; Magnesium chelatase subunit I, C-Terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR011775; Mg_chelatase_ATPase-isu.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02030; BchI-ChlI; 1.
DR PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR PANTHER; PTHR32039:SF9; MAGNESIUM-CHELATASE SUBUNIT CHLI-1, CHLOROPLASTIC; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362087};
KW Chlorophyll biosynthesis {ECO:0000256|RuleBase:RU362087};
KW Chloroplast {ECO:0000256|RuleBase:RU362087};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU362087};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362087};
KW Photosynthesis {ECO:0000256|RuleBase:RU362087};
KW Plastid {ECO:0000256|RuleBase:RU362087};
KW Reference proteome {ECO:0000313|Proteomes:UP000188354}.
FT DOMAIN 105..287
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 418 AA; 45964 MW; 6702369F2C449B91 CRC64;
MASILGTSSS IALLHSPRYS SSSIPSLSLA TGKIFRHKSY KEIGLHGIKG KSQFSVASVA
TEVNSVEQVQ KIASKESQRP VYPFSAIVGQ DEMKLCLLLN VIDPKIGGVM IMGDRGTGKS
TTVRSLVDLL PEIKVVAGDP YNSDPEDPEF MGVEVRERVI KGEQLQVVFS KINMVDLPLG
ATEDRVCGTI DIEKALTEGV KAFEPGLLAK ANRGILYVDE VNLLDDHLVD VLLDSAASGW
NTVEREGISI AHPARFILIG SGNPEEGELR PQLLDRFGMH AQVGTVRDAE LRVKIVEERS
RFDKNPKEFR DSYNAEQEKL QQQISSARSF LSSVQIDRDL KIKISKVCAE LNVDGLRGDI
VTNRAAKALA ALKQRDKVSA EDIATVIPNC LRHRLRKDPL ESIDSGLVII EKFYEVFT
//
